2ovu

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<StructureSection load='2ovu' size='340' side='right'caption='[[2ovu]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='2ovu' size='340' side='right'caption='[[2ovu]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ovu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cangl Cangl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OVU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ovu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_gladiata Canavalia gladiata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OVU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ow4|2ow4]], [[2p2k|2p2k]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ovu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ovu OCA], [http://pdbe.org/2ovu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ovu RCSB], [http://www.ebi.ac.uk/pdbsum/2ovu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ovu ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ovu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ovu OCA], [https://pdbe.org/2ovu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ovu RCSB], [https://www.ebi.ac.uk/pdbsum/2ovu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ovu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CONA_CANGL CONA_CANGL]] Glucose/D-mannose/rhamnose specific lectin. Has hemagglutinating activity towards rabbit erythrocytes. Has mitogenic activity towards murine splenocytes that is inhibited by glucose. Inhibits HIV-1 reverse transcriptase with an IC(50) of 35uM. Has a potent antiproliferative activity against L1210 leukemia cells in vitro that is not inhibited by glucose. Inhibits translation in cell-free rabbit reticulocyte system with an IC(50) of 2.08uM. Lacks anti-fungal activity against M.arachidicola, B.cenera and F.oxysporum.<ref>PMID:15935326</ref>
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[https://www.uniprot.org/uniprot/CONA_CANGL CONA_CANGL] Glucose/D-mannose/rhamnose specific lectin. Has hemagglutinating activity towards rabbit erythrocytes. Has mitogenic activity towards murine splenocytes that is inhibited by glucose. Inhibits HIV-1 reverse transcriptase with an IC(50) of 35uM. Has a potent antiproliferative activity against L1210 leukemia cells in vitro that is not inhibited by glucose. Inhibits translation in cell-free rabbit reticulocyte system with an IC(50) of 2.08uM. Lacks anti-fungal activity against M.arachidicola, B.cenera and F.oxysporum.<ref>PMID:15935326</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ovu ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ovu ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Plant lectins, especially those purified from species of the Leguminosae family, represent the best studied group of carbohydrate-binding proteins. The legume lectins from Diocleinae subtribe are highly similar proteins that present significant differences in the potency/efficacy of their biological activities. The structural studies of the interactions between lectins and sugars may clarify the origin of the distinct biological activities observed in this high similar class of proteins. In this way, this work presents a crystallographic study of the ConM and CGL (agglutinins from Canavalia maritima and Canavalia gladiata, respectively) in the following complexes: ConM/CGL:Man(alpha1-2)Man(alpha1-O)Me, ConM/CGL:Man(alpha1-3)Man(alpha1-O)Me and ConM/CGL:Man(alpha1-4)Man(alpha1-O)Me, which crystallized in different conditions and space group from the native proteins. The structures were solved by molecular replacement, presenting satisfactory values for R(factor) and R(free). Comparisons between ConM, CGL and ConA (Canavalia ensiformis lectin) binding mode with the dimannosides in subject, presented different interactions patterns, which may account for a structural explanation of the distincts biological properties observed in the lectins of Diocleinae subtribe.
 
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Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: new insights into the understanding of the structure-biological activity relationship in legume lectins.,Bezerra GA, Oliveira TM, Moreno FB, de Souza EP, da Rocha BA, Benevides RG, Delatorre P, de Azevedo WF Jr, Cavada BS J Struct Biol. 2007 Nov;160(2):168-76. Epub 2007 Aug 16. PMID:17881248<ref>PMID:17881248</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2ovu" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cangl]]
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[[Category: Canavalia gladiata]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Azevedo, W F.de]]
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[[Category: Benevides RG]]
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[[Category: Benevides, R G]]
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[[Category: Bezerra GA]]
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[[Category: Bezerra, G A]]
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[[Category: Cavada BS]]
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[[Category: Cavada, B S]]
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[[Category: Delatorre P]]
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[[Category: Delatorre, P]]
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[[Category: Moreno FBMB]]
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[[Category: Moreno, F B.M B]]
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[[Category: Da Rocha BAM]]
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[[Category: Oliveira, T M.de]]
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[[Category: De Azevedo Jr WF]]
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[[Category: Rocha, B A.M da]]
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[[Category: De Oliveira TM]]
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[[Category: Souza, E P.de]]
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[[Category: De Souza EP]]
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[[Category: Canavalia gladiata]]
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[[Category: Lectin]]
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[[Category: Man1-2mano-me]]
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[[Category: Sugar binding protein]]
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Current revision

Crystal structure of a lectin from Canavalia gladiata (CGL) in complex with man1-2man-OMe

PDB ID 2ovu

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